Evidence map›Paper›PMID 35216155›Full record

ArticleInternational journal of molecular sciences2022

The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.

Kazunori K Fujii, Yuki Taga, Yusuke K Takagi, Ryo Masuda, Shunji Hattori, Takaki Koide

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 26 citations in OpenAlex.

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  12. An innovative temperature-controlling handpiece for face and body skin laxity and tightening treatment with radiofrequency.Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI) · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Kazunori K FujiiDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Shinjuku, Tokyo 169-8555, Japan.
Yuki TagaNippi Research Institute of Biomatrix, 520-11 Kuwabara, Toride 302-0017, Japan.ORCID 0000-0001-9100-758X
Yusuke K TakagiDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Shinjuku, Tokyo 169-8555, Japan.
Ryo MasudaWaseda Research Institute for Science and Engineering, Waseda University, Shinjuku, Tokyo 169-8555, Japan.
Shunji HattoriNippi Research Institute of Biomatrix, 520-11 Kuwabara, Toride 302-0017, Japan.
Takaki KoideDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Shinjuku, Tokyo 169-8555, Japan.ORCID 0000-0002-0681-6874
Waseda University · JPJapan Institute of Leather Research · JP

Funding

Waseda University Waseda University Grant for Special Research Projects (Project number: 2020C-292)
6 · The paper itself

Abstract

Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydroxylation, and following glycosylations. The modifications, especially prolyl 4-hydroxylation, enhance the thermal stability of the procollagen triple helix. Procollagen molecules are transported to the Golgi and secreted from the cell, after the triple helix is formed in the ER. In this study, we investigated the relationship between the thermal stability of the collagen triple helix and environmental temperature. We analyzed the number of collagen post-translational modifications and thermal melting temperature and α-chain composition of secreted type I collagen in zebrafish embryonic fibroblasts (ZF4) cultured at various temperatures (18, 23, 28, and 33 °C). The results revealed that thermal stability and other properties of collagen were almost constant when ZF4 cells were cultured below 28 °C. By contrast, at a higher temperature (33 °C), an increase in the number of post-translational modifications and a change in α-chain composition of type I collagen were observed; hence, the collagen acquired higher thermal stability. The results indicate that the thermal stability of collagen could be autonomously tuned according to the environmental temperature in poikilotherms.

Indexed as

AnimalsCell LineCollagenFibroblastsProtein Conformation, alpha-HelicalProtein Processing, Post-TranslationalProtein StabilityTemperatureZebrafishCollagencollagenenvironmental temperaturepost-translational modificationthermal stabilitytriple helix

Identifiers

PMID35216155
PMCPMC8877210
OpenAlexW4213061413

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.